Glaxosmithkline Biologicals Sa

Novartis Vaccines and Diagnostics Srl

Novartis Ag

J. Craig Venter Institute

J. Craig Venture Institute, Inc.

Novartis Vaccines & Diagnostics, Gmbh

Maria Rita Fontana

Mariagrazia Pizza

Laura Serino

Danilo Gomes Moriel

Vega Masignani

Francesco Berlanda Scorza

Herve Tettelin

Nathalie Norais

Rino Rappuoli

Elisabetta Monaci

Valentina Giannelli

Vega Masiganani

Mariagrazia c/O Chiron Corporation Pizza

Danilo Novartis Vaccines Gomes Moriel

Francesco C/O Chiron Corporation Berlanda Scorza

Laura C/O Chiron Corporation Serino

Homologs of theproteins orf353, bacterial lg-like domain (group 1) protein (orf405), flu antigen 43 (orf1 364), NodT-family outer-membrane-factor-lipoprotein efflux transporter (orf1 767), gspK (orf3515), gspJ (orf3516), toriB-dependent siderophore receptor (orO597), fibrial protein (orf3613), upec-948, upec-1232. A chain precursor of the type-1 fimbria! protein (upec-1875), yapH homolog (upec-2820), hemolysin A (recp-3768), and Sel 1 repeat-containing protein (upec-521 1) from several pathogenic strains ofhave been identified with regions within the proteins that are conserved across all. Fragments corresponding to the conserved regions, especially immunogenic fragments such a linear B-epitopes, are provided. In addition, variants of the bacterial lg-like domain (group 1) protein (orf405), yapH homolog (upec2820) and two different fragments of hemolysin A (recp3768) are provided herein that have increased solubility as compared to the native protein where the variants still raise a substantially similar immune response in a subject as the corresponding native protein.

Conservedbacterial IG-like domain (group 1) protein (ORF405) immunogens

Detoxified variants of the pathogenic'AcfD precursor' (orf3526) have been identified that raise a substantially similar immune response in a subject as the native AcfD (orB526) protein. The detoxified variants may be further modified to have increased solubility as compared to the native AcfD (orf3526) protein.

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Disclosed herein are various open reading frames from a strain ofresponsible for neonatal meningitis (MNEC), and a subset of these that is of particular interest for preparing compositions for immunizing against MNEC infections.

Variants of the pathogenic'AcfD precursor' have been identified with increased solubility as compared to the native AcfD protein that raise a substantially similar immune response in a subject as the native AcfD protein.

Disclosed herein are various open reading frames from a strain ofresponsible for neonatal meningitis (MNEC), and a subset of these that is of particular interest for preparing compositions for immunising against MNEC infections.

The invention provides proteins from gonococcus (), including amino acid sequences, the corresponding nucleotide sequences, expression data, and serological data. The proteins are useful antigens for vaccines, immunogenic compositions, and/or diagnostics. They are also useful for distinguishing between gonococcus and meningococcus and, in particular, between gonococcus and serogroup B meningococcus.

Gonococcal proteins and nucleic acids

Disclosed herein are various genes that can be included in immunogenic compositions specific for pathogenicstrains. The genes are from uropathogenic strains but are absent from non-pathogenic strains, and their encoded proteins have cellular locations which render them accessible to the immune system.

An immunogenic detoxified protein comprising the amino acid sequence of subunit A of a cholera toxin (CT-A) or a fragment thereof or the amino acid sequence of subunit A of anheat labile toxin (LT-A) or a fragment thereof wherein the amino acids at, or in positions corresponding to Ser-63 and Arg-192 are replaced with another amino acid. The immunogenic detoxified protein is useful as vaccine foror an enterotoxigenic strain ofand is produced by recombinant DNA means by site-directed mutagenesis.

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Siena, Italy

Maria Rita Fontana